Munc18-1 mutations that strongly impair SNARE-complex binding support normal 
synaptic transmission.

Meijer, M.; Burkhardt, P.; de Wit, H.; Toonen, R. F.; Fasshauer, D.; Verhage, M.

doi:10.1038/emboj.2012.72

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学術論文

Munc18-1 mutations that strongly impair SNARE-complex binding support normal synaptic transmission.

MPS-Authors

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Burkhardt, P.
Research Group of Structural Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Fasshauer, D.
Research Group of Structural Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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http://www.nature.com/emboj/journal/v31/n9/pdf/emboj201272a.pdf
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引用

Meijer, M., Burkhardt, P., de Wit, H., Toonen, R. F., Fasshauer, D., & Verhage, M. (2012). Munc18-1 mutations that strongly impair SNARE-complex binding support normal synaptic transmission. The EMBO Journal, 31(9), 2156-2168. doi:10.1038/emboj.2012.72.

引用: https://hdl.handle.net/11858/00-001M-0000-000F-9B5C-1

要旨

Synaptic transmission depends critically on the Sec1p/Munc18 protein Munc18-1, but it is unclear whether Munc18-1 primarily operates as a integral part of the fusion machinery or has a more upstream role in fusion complex assembly. Here, we show that point mutations in Munc18-1 that interfere with binding to the free Syntaxin1a N-terminus and strongly impair binding to assembled SNARE complexes all support normal docking, priming and fusion of synaptic vesicles, and normal synaptic plasticity in munc18-1 null mutant neurons. These data support a prevailing role of Munc18-1 before/during SNARE-complex assembly, while its continued association to assembled SNARE complexes is dispensable for synaptic transmission.